Gustav Berggren group

Metalloproteins and their cofactors
Our research
The Berggren group is characterized by an interdisciplinary approach to bioinorganic chemistry, combining synthetic chemistry with classical biochemical and biophysical techniques, and covers a broad range of topics related to metalloproteins and their cofactors. Emphasis is placed on understanding the interactions between the peptide and the inorganic cofactor in the active site, and showing how this knowledge can be used in (bio-)technological applications.
Group members
Publications
Part of Journal of the American Chemical Society, p. 4654-4666, 2025
- DOI for Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved H2 Evolution and O2 Tolerance through Rational Design of [FeFe] Hydrogenase
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Part of Energy & Fuels, p. 4987-5006, 2025
- DOI for Outlook on Synthetic Biology-Driven Hydrogen Production: Lessons from Algal Photosynthesis Applied to Cyanobacteria
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Part of Microbial Cell Factories, 2025
- DOI for Structure-guided engineering of α-ketoisocaproate dioxygenase increases isobutene production in Synechocystis sp. PCC 6803
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Part of Physical Chemistry, Chemical Physics - PCCP, p. 9864-9875, 2025
- DOI for Indications for a universal hydrogen catalysis mechanism in [FeFe]-hydrogenases of different phylogenetic groups
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Part of Nature Communications, 2024
- DOI for Embedding biocatalysts in a redox polymer enhances the performance of dye-sensitized photocathodes in bias-free photoelectrochemical water splitting
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Kinetic Modeling of the Reversible or Irreversible Electrochemical Responses of FeFe-Hydrogenases
Part of Journal of the American Chemical Society, p. 1455-1466, 2024
Semiartificial Photosynthetic Nanoreactors for H2 Generation
Part of Journal of the American Chemical Society, p. 34260-34264, 2024
- DOI for Semiartificial Photosynthetic Nanoreactors for H2 Generation
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Part of ACS Catalysis, p. 10435-10446, 2023
- DOI for Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase
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Part of ACS Catalysis, p. 9476-9486, 2023
- DOI for Elucidating Electron Transfer Kinetics and Optimizing System Performance for Escherichia coli-Based Semi-Artificial H-2 Production
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Part of Energy Advances, p. 2085-2092, 2023
- DOI for E. coli-based semi-artificial photosynthesis: biocompatibility of redox mediators and electron donors in [FeFe] hydrogenase driven hydrogen evolution
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Structural basis for bacterial energy extraction from atmospheric hydrogen
Part of Nature, p. 541-547, 2023
- DOI for Structural basis for bacterial energy extraction from atmospheric hydrogen
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Part of Frontiers in Microbiology, 2023
- DOI for Novel concepts and engineering strategies for heterologous expression of efficient hydrogenases in photosynthetic microorganisms
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Part of ACS Catalysis, p. 1246-1256, 2023
Part of Sustainable Energy & Fuels, p. 4967-4976, 2023
- DOI for Synthetic styrene-based bioinspired model of the [FeFe]-hydrogenase active site for electrocatalytic hydrogen evolution
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Part of Journal of Biological Inorganic Chemistry, p. 345-355, 2022
- DOI for Stability of the H-cluster under whole-cell conditions—formation of an Htrans-like state and its reactivity towards oxygen
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Part of ACS Sustainable Chemistry and Engineering, p. 10760-10767, 2022
- DOI for Light-Driven [FeFe] Hydrogenase Based H-2 Production in E. coli: A Model Reaction for Exploring E. coli Based Semiartificial Photosynthetic Systems
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Part of Chemical Science, p. 11058-11064, 2022
- DOI for Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site
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Part of Journal of the American Chemical Society, p. 13600-13611, 2022
- DOI for Polymer Dots as Photoactive Membrane Vesicles for [FeFe]-Hydrogenase Self-Assembly and Solar-Driven Hydrogen Evolution
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Part of Dalton Transactions, p. 4634-4643, 2022
- DOI for Lewis acid protection turns cyanide containing [FeFe]-hydrogenase mimics into proton reduction catalysts
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Part of Chemical Communications, p. 7184-7187, 2022
- DOI for Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H-2 supports its catalytic relevance
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Part of Chemistry - A European Journal, 2022
- DOI for Non‐Covalent Integration of a [FeFe]‐Hydrogenase Mimic to Multiwalled Carbon Nanotubes for Electrocatalytic Hydrogen Evolution
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Reversible or Irreversible Catalysis of H+/H2 Conversion by FeFe Hydrogenases
Part of Journal of the American Chemical Society, p. 20320-20325, 2021
Part of Physiologia Plantarum, p. 555-567, 2021
- DOI for Photosynthetic hydrogen production: Novel protocols, promising engineering approaches and application of semi‐synthetic hydrogenases
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Semi-synthetic hydrogenases—in vitro and in vivo applications
Part of Current Opinion in Green and Sustainable Chemistry, 2021
- DOI for Semi-synthetic hydrogenases—in vitro and in vivo applications
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Part of Cell Reports Physical Science, 2021
- DOI for Semisynthetic [FeFe]-hydrogenase with stable expression and H2 production capacity in a photosynthetic microbe
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Part of Journal of Biological Inorganic Chemistry, p. 571-582, 2020
- DOI for The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron
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Part of ACS Catalysis, p. 9943-9952, 2020
- DOI for Carbon Dots and [FeFe] Hydrogenase Biohybrid Assemblies for Efficient Light-Driven Hydrogen Evolution
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Part of Chemical Science, p. 12789-12801, 2020
- DOI for Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture
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Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations
Part of ACS Catalysis, p. 7069-7086, 2020
Part of Chemical Science, p. 4608-4617, 2020
- DOI for Spectroscopic investigations under whole-cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase
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The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
Part of Journal of Biological Chemistry, p. 11891-11901, 2020
- DOI for The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
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Part of Journal of Biological Inorganic Chemistry, p. 777-788, 2020
- DOI for [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy
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Part of Dalton Transactions, p. 858-865, 2020
- DOI for The reactivity of molecular oxygen and reactive oxygen species with [FeFe] hydrogenase biomimetics: reversibility and the role of the second coordination sphere
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Part of Chemical Science, p. 5582-5588, 2019
- DOI for Metal vs. ligand protonation and the alleged proton-shuttling role of the azadithiolate ligand in catalytic H-2 formation with FeFe hydrogenase model complexes
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Part of Journal of Biological Inorganic Chemistry, p. 841-848, 2019
- DOI for Compounds with capacity to quench the tyrosyl radical in Pseudomonas aeruginosa ribonucleotide reductase
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Synthesis of a miniaturized [FeFe] hydrogenase model system
Part of Dalton Transactions, p. 2280-2284, 2019
- DOI for Synthesis of a miniaturized [FeFe] hydrogenase model system
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Part of Journal of Biological Inorganic Chemistry, p. 849-861, 2019
- DOI for Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access
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Discovery of novel [FeFe]-hydrogenases for biocatalytic H-2-production
Part of Chemical Science, p. 9941-9948, 2019
- DOI for Discovery of novel [FeFe]-hydrogenases for biocatalytic H-2-production
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Monitoring H-cluster assembly using a semi-synthetic HydF protein
Part of Dalton Transactions, p. 5978-5986, 2019
Part of Journal of Biological Inorganic Chemistry, p. 863-877, 2019
- DOI for Class Id ribonucleotide reductase utilizes a Mn2(IV,III) cofactor and undergoes large conformational changes on metal loading
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Part of Faraday discussions, p. 162-174, 2019
- DOI for Photoinduced hole transfer from tris(bipyridine)ruthenium dye to a high-valent iron-based water oxidation catalyst
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Efficient visible light-driven water oxidation catalysed by an iron(IV) clathrochelate complex
Part of Chemical Communications, p. 3335-3338, 2019
- DOI for Efficient visible light-driven water oxidation catalysed by an iron(IV) clathrochelate complex
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Part of Sustainable Energy & Fuels, p. 724-750, 2018
- DOI for From protein engineering to artificial enzymes - biological and biomimetic approaches towards sustainable hydrogen production
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Part of eLIFE, 2018
- DOI for Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit
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Part of Journal of Biological Chemistry, p. 15889-15900, 2018
- DOI for A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant
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InVivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases
Part of Angewandte Chemie International Edition, p. 2596-2599, 2018
Part of Inorganic Chemistry, p. 10424-10430, 2018
Hydrogen evolution by a photoelectrochemical cell based on a Cu2O-ZnO-[FeFe] hydrogenase electrode
Part of Journal of Photochemistry and Photobiology A, p. 27-33, 2018
- DOI for Hydrogen evolution by a photoelectrochemical cell based on a Cu2O-ZnO-[FeFe] hydrogenase electrode
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Generation of a functional, semisynthetic [FeFe]-hydrogenase in a photosynthetic microorganism
Part of Energy & Environmental Science, p. 3163-3167, 2018
- DOI for Generation of a functional, semisynthetic [FeFe]-hydrogenase in a photosynthetic microorganism
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In vivo activation of an [FeFe] hydrogenase using synthetic cofactors
Part of Energy & Environmental Science, p. 1563-1567, 2017
- DOI for In vivo activation of an [FeFe] hydrogenase using synthetic cofactors
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